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AIYAR, STEPHAN GRISSMER, AND K. GEORGE CHANDY California 92717 of Physiology and Biophysics, University of California, Irvine, JAYASHREE Aiyar, Jayashree, Stephan Grissmer, and K. George Chandy. Full-length and truncated Kvl.3 are modulatedby 5-HT1, receptor activation and independently by PKC. Am. J. Physiol. 265 (Cell Physiol. 34): Cl571-Cl578, 1993.-In T-cells, the Shaker-related gene,Kvl.3 encodes the type n K+ channel, whereasthe type 1channel is a product of the Shaw subfamily gene, Kv3.1. Both these genes are also expressed the brain. We have usedthe Xenopus oocyte hetin erologous expressionsystemto study the modulatory effects of serotonin (5-hydroxytryptamine, 5-HT) on both these cloned channels.In oocytes coexpressingthe mouse5-HT1, receptor and mouseKvl.3 channel, addition of 100 nM 5-HT causes a complete and sustainedsuppression Kvl.3 currents in -20 of min. In contrast, 5-HT has no effect on mouseKv3.1 currents when coexpressed with 5-HT1, receptor. The 5-HT-mediated suppression Kvl.3 currents proceedsvia activation of a perof tussistoxin-sensitive G protein and a subsequent rise in intracellular Ca2+, but Ca2+ does not directly block the channel. Protein kinase (PK) C activation is not part of the pathway linking 5-HT1, receptor to Kvl.3 channels. However, phorbol estersindependently suppress Kvl.3 currents. Deletion of the first 146 amino acidsfrom the NH,-terminal, containing putative
AJP - Cell Physiology – The American Physiological Society
Published: Dec 1, 1993
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